Zinc-Alpha-2-Glycoprotein Human HEK293

Cat. No.	Size	Price
RD172093025	0.025 mg
RD172093100	0.1 mg

Technical Data

Type

Recombinant protein

Description

Total 291AA, 33,5 kDa (computed). The AA sequence (14–291) is identical to Swiss-Prot-P25311 (AA18–295 mature Zinc-Alfa-2-Glycoprotein). THIRTEEN extra amino acid were fused with N-terminus (highlighted).

Amino Acid Sequence

PGDYKDDDDKPAGQENQDGRYSLTYIYTGLSKHVEDVPAFQALGSLNDLQFFRYNSKDRKSQPMGLWRQVEGMEDWKQDSQLQKAREDIFMETLKDIVEYYNDSNGSHVLQGRFGCEIENNRSSGAFWKYYYDGKDYIEFNKEIPAWVPFDPAAQITKQKWEAEPVYVQRAKAYLEEECPATLRKYLKYSKNILDRQDPPSVVVTSHQAPGEKKKLKCLAYDFYPGKIDVHWTRAGEVQEPELRGDVLHNGNGTYQSWVVVAVPPQDTAPYSCHVQHSSLAQPLVVPWEAS

Source

HEK293

Purity

Purity as determined by densitometric image analysis: >90%

SDS-PAGE Gel

12% SDS-PAGE separation of Human ZA2G
1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
2. reduced and heated sample, 10μg/lane
3. non-reduced and non-heated sample, 10μg/lane

Endotoxin

< 0.1 EU/ug

Formulation

Filtered (0,4 μm) and lyophilized in 0.5 mg/mL in 20mM TRIS, 50mM NaCl, pH 7.5

Reconstitution

Add deionized water to prepare a working stock solution of 0.5 mg/mL and let the lyophilized pellet dissolve completely. Filter sterilize your culture media/working solutions containing this non-sterile product before using in cell culture.

Applications

Western blotting, ELISA, Cell culture and/or animal studies

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store lyophilized protein at –80°C. Lyophilized protein remains stable until the expiry date when stored at –80°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80°C for long term storage. Reconstituted protein can be stored at 4°C for a week.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.

Summary

Research topic

Energy metabolism and body weight regulation, Oncology

Summary

Zinc-alpha-2-glycoprotein (ZAG) is found in body fluids such as serum, sweat, and seminal and breast cyst fluids. It is identical in amino acid sequence to tumor-derived lipid mobilizing factor (LMF), a protein associated with the dramatic loss of adipose body stores in cancer cachexia, and has been shown to stimulate lipolysis by adipocytes in vivo and in vitro. A role for ZAG has been proposed in the regulation of body weight, and age-dependent changes in genetically influenced obesity, and also it regulates melanin production by normal and malignant melanocytes. It has also recently been classified as a novel adipokine in that it is produced by both white and brown fat adipocytes and may act in a local autocrine fashion in the reduction of adiposity in cachexia. Controlling ZAG/LMF's activity could be life-saving in the management of certain cancers and other cachexia-inducing conditions, and its possible normal role in body fat store homeostasis is deserving of understanding in its own right. ZAG exhibits a class I major histocompatibility complex (MHC) fold but is a soluble protein rather than being anchored to plasma membranes and does not associate with alpha-2-microglobulin in humans. Like antigen-presenting MHC class I proteins, ZAG has an open apical groove, and X-ray crystallography of human-derived ZAG revealed an unidentifiable electron density in a similar position to that occupied by antigenic peptides in classical MHC proteins and glycolipids in isoforms of CD1. This presumptive ligand is not a peptide, and the groove is too small to hold a glycolipid such as is presented by CD1 isoforms. By analogy with all other MHC class I-related proteins that have an open apical groove [some do not ], occupancy by a ligand is probably crucial to ZAG's biological function. Despite all of the structural and biochemical evidence that ZAG binds a ligand, none has so far been found by extraction from protein isolated from biological fluids. This difficulty could be because the ligand is labile, heterogeneous, or readily lost during purification procedures. Knowing more about how ZAG interacts with the compounds it has been found to bind, both natural and artificial, will inform searches for the elusive ligand(s) and its/their role in ZAG's signaling function.

Product References (2)

References

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Gordon SC, Polson DJ, Shirkhoda A. Budd-Chiari syndrome complicatingpre-eclampsia: diagnosis by magnetic resonance imaging. J Clin Gastroenterol.1991 Aug;13(4):460-2. PubMed PMID: 1918855. See more on PubMed

Summary References (19)

References to Zinc-Alpha-2-Glycoprotein

Araki T, Gejyo F, Takagaki K, Haupt H, Schwick HG, Burgi W, Marti T, Schaller J, Rickli E, Brossmer R, et al. Complete amino acid sequence of human plasma Zn-alpha 2-glycoprotein and its homology to histocompatibility antigens. Proc Natl Acad Sci U S A. 1988 Feb;85 (3):679-83
Bao Y, Bing C, Hunter L, Jenkins JR, Wabitsch M, Trayhurn P. Zinc-alpha2-glycoprotein, a lipid mobilizing factor, is expressed and secreted by human (SGBS) adipocytes. FEBS Lett. 2005 Jan 3;579 (1):41-7
Bennett MJ, Lebron JA, Bjorkman PJ. Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor. Nature. 2000 Jan 6;403 (6765):46-53
Bing C, Bao Y, Jenkins J, Sanders P, Manieri M, Cinti S, Tisdale MJ, Trayhurn P. Zinc-alpha2-glycoprotein, a lipid mobilizing factor, is expressed in adipocytes and is up-regulated in mice with cancer cachexia. Proc Natl Acad Sci U S A. 2004 Feb 24;101 (8):2500-5
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Brysk MM, Lei G, Selvanayagam P, Brysk H, Tyring SK, Arany I. Modulation by interferon-gamma of zinc-alpha 2-glycoprotein gene expression in human epithelial cell lines. Anticancer Res. 1997 Sep-Oct;17 (5A):3387-91
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Hale LP. Zinc alpha-2-glycoprotein regulates melanin production by normal and malignant melanocytes. J Invest Dermatol. 2002 Aug;119 (2):464-70
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